Research workbench

Crystal structure of hypothetical protein APE1520 from aeropyrum pernix K1

Analyse Crystal structure of hypothetical protein APE1520 from aeropyrum pernix K1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2P6H
Type: protein
Length: 268 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hypothetical protein
UniProt: Q9YBS9
Ligands: SO4
Pockets: 1 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Hypothetical protein	protein	134	28% helix, 37% strand	Q9YBS9

Ligands and binding sites

SO4 · Sulfate ion · ion · 6 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	555	0.76	0.83	59	empty

Interfaces

1 interface between chains.

A–B · 665 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

2P6H · Crystal structure of hypothetical protein APE1520 from Aeropyrum pernix K1 · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q9YBS9
Elsewhere: RCSB PDB 2P6H · PDBe 2P6H · UniProt Q9YBS9

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